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Nucleic Acids Research, 1993, Vol. 21, No. 2 303-309
© 1993

ENZYMOLOGY

Sequence-specific and mechanism-based crosslinking of Dcm DNA cytosine-C5 methyltransferase of E.coli K-12 to synthetic oligonucleotides containing 5-fluoro-2'-deoxycytidine

Theodor Hanck, Sabine Schmidt1 and Hans-Joachim Fritz*

Institut für Molekulare Genetik, Georg-August-Universität Göttingen Grisebachstrae 8, W-3400 Göttingen 1Institut für Bioorganische Chemie, Humboldt- Universität Berlin Invalidenstraße 42, O-1040 Berlin 33, Germany

*To whom correspondence should be addressed

Received September 13, 1992. Revised November 8, 1992. Accepted November 8, 1992.

The product of the dcm gene Is the only DNA cytosine C5 methyltransferase of Escherlchla coli K-12; it catalyses transfer of a methyl group from Sadenosyl methlonine (SAM) to the C-5 position of the inner cytosine residue of the cognate sequence CCATGG. Sequence-specific, covalent crosslinking of the enzyme to synthetic oligonucleotides containing 5-fluoro-2'-deoxycytidine is demonstrated. This reaction is abolished if serine replaces the cysteine at residue 177 of the enzyme. These results lend strong support to a catalytic mechanism in which an enzyme sulfhydryl group undergoes Michael addition to the C5-C6 double bond, thus activating position C-5 of the substrate DNA cytosine residue for electrophllic attack by the methyl donor SAM. The enzyme is capable of self-methylatlon in a DNA-independent reaction requiring SAM and the presence of cysteine at position 177.


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